Wang J F, Hampton B, Mehlman T, Burgess W H, Rechler M M
Molecular, Cellular and Nutritional Endocrinology Branch, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20892.
Biochem Biophys Res Commun. 1988 Dec 15;157(2):718-26. doi: 10.1016/s0006-291x(88)80309-7.
We have purified a 14 kDa fragment of the 30 kDa binding protein for insulin-like growth factors (IGFs) from BRL-3A cell conditioned medium. The fragment binds IGF-I and IGF-II with similar specificity to the 30 kDa binding protein, but with lower affinity. It corresponds to the carboxy terminus of the native binding protein (residues 148-270), and is thought to arise by proteolysis. We infer that this region of the native binding protein contains, at least in part, the IGF binding domain.
我们从BRL - 3A细胞条件培养基中纯化出了一种用于胰岛素样生长因子（IGFs）的30 kDa结合蛋白的14 kDa片段。该片段与IGF - I和IGF - II结合的特异性与30 kDa结合蛋白相似，但亲和力较低。它对应于天然结合蛋白的羧基末端（第148 - 270位氨基酸残基），被认为是由蛋白水解产生的。我们推断天然结合蛋白的这一区域至少部分包含IGF结合结构域。
